scholarly journals Sequence of the full-length immunoglobulin κ-chain of mouse myeloma MPC 11

1978 ◽  
Vol 171 (2) ◽  
pp. 337-347 ◽  
Author(s):  
G P Smith
Keyword(s):  
Variable Region ◽  
Full Length ◽  
Light Chains ◽  
Its Sequence ◽  
Heavy Chains ◽  
Immunoglobulin Kappa ◽  
N Terminus ◽  
Kappa Chain ◽  
Kappa Light Chains ◽  
Mouse Myeloma

MPC 11 mouse myeloma cells synthesize two immunoglobulin kappa light chains, coded by two separate genes. One of these Kappa-chains has no variable region and is degraded intracellularly. The other is a full-length kappa-chain contaning both variable and constant regions: this chain is secreted, both by itself and combined with heavy chains in molecules of immunoglobulin G. This paper reports the amino acid sequence of the myeloma MPC 11 full-length kappa-chain. The chain is unusual in having 12 extra residues at its N-terminus when its sequence is aligned with those of other mouse kappa-chains; no other anomalies were found in its sequence.

scholarly journals Clonal nature of the immune response to phosphorylcholine (PC). V. Cross-idiotypic specificity among heavy chains of murine anti-PC antibodies and PC-binding myeloma proteins.

1975 ◽  
Vol 141 (5) ◽  
pp. 1073-1083 ◽  
Author(s):  
J L Claflin ◽  
J M Davie
Keyword(s):  
Heavy Chain ◽  
Antigenic Determinant ◽  
Variable Region ◽  
Antigenic Determinants ◽  
Genetic Origin ◽  
Heavy Chains ◽  
Myeloma Proteins ◽  
Kappa Chain ◽  
Clonal Nature ◽  
Mouse Myeloma

Seven mouse myeloma proteins with specificity for phosphorylcholine (PC) were found to share a common antigenic determinant. This group of proteins contained members which differed in genetic origin, heavy chain class, kappa-chain subgroup, individual antigenic determinants and specificity for choline analogues. The cross-idiotypic determinant, VH-PC, was antigenically similar in each of the proteins and was associated with the variable portion of the heavy chain in the region of the antibody combining site. Further studies showed that an indistinguishable determinant was present on IgM anti-PC antibodies isolated from all strains of mice tested regardless of histocompatibility or heavy chain allotype. In view of the finding that this cross-idiotypic determinant was not found on antibodies or myeloma proteins which lacked specificity for PC, the data strongly suggest that a particular heavy chain variable region has been preserved in all mouse antibodies with specificity for PC.

scholarly journals Sequence of a cDNA encoding Basilea kappa light chains (K2 isotype) suggests a possible relationship of protein structure to limited expression.

1984 ◽  
Vol 159 (2) ◽  
pp. 635-640 ◽  
Author(s):  
K E Bernstein ◽  
E Lamoyi ◽  
N McCartney-Francis ◽  
R G Mage
Keyword(s):  
Sulfhydryl Group ◽  
Variable Region ◽  
Complete Sequence ◽  
Light Chains ◽  
Small Subset ◽  
Constant Region ◽  
Region Gene ◽  
Variable Regions ◽  
Immunoglobulin Kappa ◽  
Kappa Light Chains

We present the complete sequence of a cDNA encoding rabbit immunoglobulin kappa light chains of the Basilea isotype (K2). Although all rabbits seem to possess a K2 constant region gene, expression of this gene in most rabbits is minimal if present at all. Even in Basilea rabbits the majority of expressed immunoglobulins are of lambda type. We find that the sequence of our Basilea cDNA constant region and the sequence of a "silent" K2 gene from b4 rabbits (bas-N4) are almost identical. The bas (K2) isotype lacks cysteine at position 171 in the constant region that is present in all K1 constant regions and usually forms an interdomain disulfide bond, with a cysteine at position 80 of the variable region. We postulate that one factor contributing to the low expression of the bas (K2) isotype could be a paucity of V kappa regions lacking cysteine at position 80. If a typical rabbit V kappa encoding Cys at position 80 is rearranged and expressed with th K2 isotype. B cells with mRNAs encoding light chains with free sulfhydryl groups would result. These cells may fail to form functional immunoglobulin receptors. Only a small subset of rabbit variable regions that lack the cysteine at position 80 would rearrange and encode K2 light chains lacking a free sulfhydryl group.

scholarly journals Expression of a public idiotype by human monoclonal IgM directed to myelin-associated glycoprotein and characterization of the variability subgroup of their heavy and light chains.

1989 ◽  
Vol 170 (5) ◽  
pp. 1551-1558 ◽  
Author(s):  
J C Brouet ◽  
K Dellagi ◽  
M C Gendron ◽  
A Chevalier ◽  
C Schmitt ◽  
...  
Keyword(s):  
Nonhuman Primate ◽  
Light Chains ◽  
Antibody Activity ◽  
Rheumatoid Factors ◽  
Variable Regions ◽  
Cold Agglutinins ◽  
Heavy Chains ◽  
Myelin Associated Glycoprotein ◽  
Kappa Light Chains

Most studies using rabbit or mouse antisera failed to detect CRI between human IgM directed to MAG. We show here that 9 of 10 such IgM express a public CRI as defined by a nonhuman primate antiserum. Shared idiotype is likely involved in (or close to) the combining site of those IgM since antiidiotypic serum inhibited the binding of IgM to MAG and reacted with IgM having different variable regions of light and heavy chains. Partial aminoterminal sequence of heavy and light chains showed that anti-MAG IgM use either lambda chains (one IgM) or kappa light chains (six IgM) of different variability subgroups (V kappa IV in three instances, V kappa I in two, and V kappa II in one), whereas heavy chains belong to the VHIII (six IgM) or to the VHII (1 IgM) subgroup. These features distinguish these IgM from other human monoclonal IgM with a defined antibody activity, such as rheumatoid factors or cold agglutinins.

scholarly journals Variable region sequences of murine IgM anti-IgG monoclonal autoantibodies (rheumatoid factors). A structural explanation for the high frequency of IgM anti-IgG B cells.

1986 ◽  
Vol 164 (2) ◽  
pp. 407-427 ◽  
Author(s):  
M J Shlomchik ◽  
D A Nemazee ◽  
V L Sato ◽  
J Van Snick ◽  
D A Carson ◽  
...  
Keyword(s):  
B Cells ◽  
Variable Region ◽  
Amino Acid Sequences ◽  
Light Chains ◽  
Binding Interaction ◽  
Structural Explanation ◽  
Region Gene ◽  
Unique Type ◽  
Heavy Chains ◽  
Germline Genes

The nucleotide sequences of heavy and light chains from 10 monoclonal IgM anti-IgG1 (RF) antibodies were determined and reported here as translated amino acid sequences. Only three families of VK light chains were used in these antibodies: VK1 (two examples), VK8 (three examples), and VK19 (four examples). This represents a significant nonrandom selection of light chains. In contrast, all other variable region gene segments (i.e., VH, DH, JH, and JK) were used in a pattern consistent with random selection from the available pool of germline genes. In two cases, the same anti-IgG1 specificity was generated by a combination of very homologous light chains with unrelated heavy chains. We infer from this that the light chain is the segment used by these antibodies to bind IgG1. The nature of these sequences provides an explanation for the curious observation that as many as 15% of splenic B cells in normal mice may be expressing IgM anti-IgG; if, as our data suggest, certain light chains in combination with many different heavy chains can be used in assembling the anti-IgG specificity, then, because of combinatorial association in which the heavy chain is not relevant for specificity, the fraction of IgM-producing B cells expressing these light chains should approximate the fraction of B cells making IgM anti-IgG. We calculate, based on data presented in several other studies, that 5-17% of B cells express one of the VK types observed in monoclonal RF. This agrees well with estimates for the number of B cells making IgM anti-IgG. In addition, our findings could rule out other explanations of the high percentage of B cells making RF, such as constant stimulation by antigen or presence of numerous antigenic epitopes since it was shown that IgM anti-IgG1 antibodies are not somatically mutated and that they are structurally homogeneous. We aligned the VK sequences of the RF in hopes of finding some primary sequence homology between the represented VK families which might point to residues involved in the binding interaction. Although we found no such homology in the hypervariable regions, we did find significant and unexpected homology in the FR2 and FR3 of these light chains. We noted that these regions are exposed in the Ig structure and postulate that they may be involved in a unique type of binding interaction between two Ig family domains, i.e., VK binding to a constant region domain of IgG.

scholarly journals Amino acid-sequence variability at the N-terminal extra piece of mouse immunoglobulin light-chain precursors of the same and different subgroups

1976 ◽  
Vol 157 (1) ◽  
pp. 145-151 ◽  
Author(s):  
Y Burstein ◽  
I Schechter
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Variable Region ◽  
Amino Acid Residues ◽  
Free System ◽  
Methionine Residue ◽  
N Terminus ◽  
Mouse Myeloma

The proteins programmed in the wheat-germ cell-free system by the mRNA coding for the MOPC-63 mouse myeloma L (light) chain were labelled with six radioactive amino acids: [35S]methionine, [4,5-3H]leucine, [3,4-3H]proline, [3-3H]serine, [4,5-3H]isoleucine or [2,3-3H]alanine. Amino acid-sequence analyses showed that over 90% of the total cell-free product was one homogeneous protein, which corresponds to the MOPC-63 L-chain precursor. In this precursor an extra piece, 20 amino acid residues in length, precedes the N-terminus of the mature L chain. The extra piece contains one methionine residue at the N-terminus, six leucine residues, which are clustered in two triplets at positions 6, 7, 8 and 11, 12, 13, one proline residue at position 16, and one serine residue at position 18. The closely gathered leucine residues, as well as their abundance (30%), suggest that the extra-piece moiety is hydrophobic. In the precursors, the extra piece is coupled to the variable region of the L chain. Partial sequences of precursors of L chains of the same and different subgroups that were labelled with the above six radioactive amino acids indicate that the extra piece is part of the variable region. Thus the precursors of MOPC-63 and MOPC-321 L chains, which are of the same subgroup, have extra pieces of identical size (20 residues), and so far their partial sequences are also identical (see above). On the other hand, in the precursor of MOPC-41 L chain, which is of a different subgroup, the extra piece is 22 residues in length. Further, the sequence of the MOPC-41 extra piece differs in at least ten positions from sequences of the extra pieces of the precursors of MOPC-63 and MOPC-321 L chains.

scholarly journals Characterization of a unique conformational epitope on free immunoglobulin kappa light chains that is recognized by an antibody with therapeutic potential

2011 ◽  
Vol 48 (9-10) ◽  
pp. 1245-1252 ◽  
Author(s):  
Andrew T. Hutchinson ◽  
Ralitza Alexova ◽  
Vanessa Bockhorni ◽  
Paul A. Ramsland ◽  
Darren R. Jones ◽  
...  
Keyword(s):  
Therapeutic Potential ◽  
Conformational Epitope ◽  
Light Chains ◽  
Immunoglobulin Kappa ◽  
Kappa Light Chains

scholarly journals The amino acid sequences of the Fd fragments of two human γ 1 heavy chains

1970 ◽  
Vol 117 (4) ◽  
pp. 641-660 ◽  
Author(s):  
E. M. Press ◽  
N. M. Hogg
Keyword(s):  
Amino Acid ◽  
Aspartic Acid ◽  
Heavy Chain ◽  
Variable Region ◽  
Amino Acid Sequences ◽  
Light Chains ◽  
Aspartic Acid Residue ◽  
Variable Regions ◽  
Heavy Chain Variable Region ◽  
Heavy Chains

The amino acid sequences of the Fd fragments of two human pathological immunoglobulins of the immunoglobulin G1 class are reported. Comparison of the two sequences shows that the heavy-chain variable regions are similar in length to those of the light chains. The existence of heavy chain variable region subgroups is also deduced, from a comparison of these two sequences with those of another γ 1 chain, Eu, a μ chain, Ou, and the partial sequence of a fourth γ 1 chain, Ste. Carbohydrate has been found to be linked to an aspartic acid residue in the variable region of one of the γ 1 chains, Cor.

scholarly journals Synthesis of abnormal heavy chains in Bence-Jones plasma cell leukemia with intracellular IgG

Blood ◽  
1980 ◽  
Vol 56 (6) ◽  
pp. 1136-1140
Author(s):  
JL Preud'homme ◽  
S Labaume ◽  
V Praloran
Keyword(s):  
Plasma Cell ◽  
Slow Rate ◽  
Plasma Cells ◽  
Plasma Cell Leukemia ◽  
Light Chains ◽  
Immunofluorescence Study ◽  
Cell Leukemia ◽  
Bence Jones Protein ◽  
Heavy Chains ◽  
Kappa Chain

In a patient with plasma cell leukemia and a kappa type Bence Jones protein in serum and urine, the immunofluorescence study of blood plasma cells showed intracellular gamma and kappa chain determinants. Biosynthesis experiments showed the production of abnormally short heavy chains (45,000 daltons) that assembled with normal sized light chains with a partial block. These abnormal heavy chains were secreted at a slow rate and were degraded after secretion.

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